首页> 美国卫生研究院文献>Journal of Bacteriology >A 20-kilodalton protein preserves cell viability and promotes CytA crystal formation during sporulation in Bacillus thuringiensis.
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A 20-kilodalton protein preserves cell viability and promotes CytA crystal formation during sporulation in Bacillus thuringiensis.

机译:在苏云金芽孢杆菌的孢子形成过程中一种20公斤的蛋白质保留了细胞活力并促进CytA晶体形成。

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摘要

The effect of a 20-kDa protein on cell viability and CytA crystal production in its natural host, Bacillus thuringiensis, was studied by expressing the cytA gene in the absence or presence of this protein. In the absence of the 20-kDa protein, B. thuringiensis cells either were killed during sporulation (strain cryB) or produced very small CytA crystals (strain 4Q7). Expression of cytA in the presence of the 20-kDa protein, however, preserved cell viability, especially in strain cryB, and in both strains yielded bipyramidal crystals of the CytA protein that were larger than those of wild-type B. thuringiensis. These results suggest that the 20-kDa protein promotes crystal formation, perhaps by chaperoning CytA molecules during synthesis and crystallization, concomitantly preventing the CytA protein from interacting lethally with the bacterial host cell.
机译:通过在不存在或存在这种蛋白的情况下表达cytA基因,研究了20 kDa蛋白对其自然宿主苏云金芽孢杆菌细胞活力和CytA晶体产生的影响。在缺乏20 kDa蛋白的情况下,苏云金芽孢杆菌细胞在孢子形成过程中被杀死(cryB株),或者产生了非常小的CytA晶体(4Q7株)。然而,在20kDa蛋白存在下cytA的表达可以保持细胞活力,尤其是在cryB菌株中,并且在两种菌株中均能产生CytA蛋白的双锥体晶体,其晶体比野生型苏云金芽孢杆菌要大。这些结果表明20-kDa蛋白可能通过在合成和结晶过程中陪伴CytA分子来促进晶体形成,从而防止CytA蛋白与细菌宿主细胞致命地相互作用。

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